ausblenden:
Schlagwörter:
ATP-Binding Cassette Transporters/chemistry/genetics/*metabolism
ATP-Dependent Proteases
Adenosine Triphosphatases/metabolism
Adenosine Triphosphate/metabolism
Carrier Proteins/metabolism
Cell Fractionation
Intracellular Membranes/*metabolism
Membrane Proteins/chemistry/metabolism
*Membrane Transport Proteins
Metalloendopeptidases/metabolism
Mitochondria/*metabolism
Mitochondrial Membrane Transport Proteins
Molecular Weight
Peptides/chemistry/*metabolism
Point Mutation
*Protein Transport
*Repressor Proteins
Saccharomyces cerevisiae/genetics/*metabolism/ultrastructure
*Saccharomyces cerevisiae Proteins
Zusammenfassung:
ATP-binding cassette (ABC) adenosine triphosphatases actively transport a wide variety of compounds across biological membranes. Here, the ABC protein Mdl1 was identified as an intracellular peptide transporter localized in the inner membrane of yeast mitochondria. Mdl1 was required for mitochondrial export of peptides with molecular masses of approximately 2100 to 600 daltons generated by proteolysis of inner-membrane proteins by the m-AAA protease in the mitochondrial matrix. Proteolysis by the i-AAA protease in the intermembrane space led to the release of similar-sized peptides independent of Mdl1. Thus, two pathways of peptide efflux from mitochondria exist that may allow communication between mitochondria and their cellular environment.
